메뉴 건너뛰기




Volumn 75, Issue , 2013, Pages 506-516

Connexin targeting peptides as inhibitors of voltage- and intracellular Ca2+-triggered Cx43 hemichannel opening

Author keywords

Channel gating; Connexin hemichannel; Connexin mimetic peptide; Gap junction; Intracellular calcium

Indexed keywords

CALMODULIN; CONNEXIN 43; GAP JUNCTION PROTEIN; GAP19 PROTEIN; GAP26 PROTEIN; GAP27 PROTEIN; L2 PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL;

EID: 84890433663     PISSN: 00283908     EISSN: 18737064     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2013.08.021     Document Type: Review
Times cited : (107)

References (103)
  • 1
    • 84870063171 scopus 로고    scopus 로고
    • Evolutionary analyses of gap junction protein families
    • F. Abascal, and R. Zardoya Evolutionary analyses of gap junction protein families Biochim. Biophys. Acta 1828 2013 4 14
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 4-14
    • Abascal, F.1    Zardoya, R.2
  • 2
    • 84873286767 scopus 로고    scopus 로고
    • Functional requirement for a highly conserved charged residue at position 75 in the gap junction protein connexin 32
    • C.K. Abrams, M. Islam, R. Mahmoud, T. Kwon, T.A. Bargiello, and M.M. Freidin Functional requirement for a highly conserved charged residue at position 75 in the gap junction protein connexin 32 J. Biol. Chem. 288 2013 3609 3619
    • (2013) J. Biol. Chem. , vol.288 , pp. 3609-3619
    • Abrams, C.K.1    Islam, M.2    Mahmoud, R.3    Kwon, T.4    Bargiello, T.A.5    Freidin, M.M.6
  • 3
    • 79959332086 scopus 로고    scopus 로고
    • Atomic force microscopy of Connexin40 gap junction hemichannels reveals calcium-dependent three-dimensional molecular topography and open-closed conformations of both the extracellular and cytoplasmic faces
    • M.J. Allen, J. Gemel, E.C. Beyer, and R. Lal Atomic force microscopy of Connexin40 gap junction hemichannels reveals calcium-dependent three-dimensional molecular topography and open-closed conformations of both the extracellular and cytoplasmic faces J. Biol. Chem. 286 2011 22139 22146
    • (2011) J. Biol. Chem. , vol.286 , pp. 22139-22146
    • Allen, M.J.1    Gemel, J.2    Beyer, E.C.3    Lal, R.4
  • 4
    • 0015142234 scopus 로고
    • Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons
    • C.M. Armstrong Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons J. Gen. Physiol. 58 1971 413 437
    • (1971) J. Gen. Physiol. , vol.58 , pp. 413-437
    • Armstrong, C.M.1
  • 5
    • 84861618268 scopus 로고    scopus 로고
    • Voltage-Dependent conformational changes in connexin channels
    • T.A. Bargiello, Q. Tang, S. Oh, and T. Kwon Voltage-dependent conformational changes in connexin channels Biochim. Biophys. Acta 1818 2012 1807 1822
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1807-1822
    • Bargiello, T.A.1    Tang, Q.2    Oh, S.3    Kwon, T.4
  • 6
    • 80054031099 scopus 로고    scopus 로고
    • + ions combine with taurine or other aminosulfonates to close Cx26 channels
    • + ions combine with taurine or other aminosulfonates to close Cx26 channels J. Gen. Physiol. 138 2011 377 380
    • (2011) J. Gen. Physiol. , vol.138 , pp. 377-380
    • Bennett, M.V.1
  • 8
    • 84883517761 scopus 로고    scopus 로고
    • Interfering amino terminal peptides and functional implications for heteromeric gap junction formation
    • E.C. Beyer, X. Lin, and R.D. Veenstra Interfering amino terminal peptides and functional implications for heteromeric gap junction formation Front Pharmacol. 4 2013 67
    • (2013) Front Pharmacol. , vol.4 , pp. 67
    • Beyer, E.C.1    Lin, X.2    Veenstra, R.D.3
  • 9
    • 0037282379 scopus 로고    scopus 로고
    • The voltage sensor and the gate in ion channels
    • F. Bezanilla, and E. Perozo The voltage sensor and the gate in ion channels Adv. Protein Chem. 63 2003 211 241
    • (2003) Adv. Protein Chem. , vol.63 , pp. 211-241
    • Bezanilla, F.1    Perozo, E.2
  • 10
    • 71749094770 scopus 로고    scopus 로고
    • Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains
    • D. Bouvier, G. Spagnol, S. Chenavas, F. Kieken, H. Vitrac, S. Brownell, A. Kellezi, V. Forge, and P.L. Sorgen Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains J. Biol. Chem. 284 2009 34257 34271
    • (2009) J. Biol. Chem. , vol.284 , pp. 34257-34271
    • Bouvier, D.1    Spagnol, G.2    Chenavas, S.3    Kieken, F.4    Vitrac, H.5    Brownell, S.6    Kellezi, A.7    Forge, V.8    Sorgen, P.L.9
  • 11
    • 0242380340 scopus 로고    scopus 로고
    • Pharmacological sensitivity of ATP release triggered by photoliberation of inositol-1,4,5-trisphosphate and zero extracellular calcium in brain endothelial cells
    • K. Braet, S.A. speslagh, W. Vandamme, K. Willecke, P.E. Martin, W.H. Evans, and L. Leybaert Pharmacological sensitivity of ATP release triggered by photoliberation of inositol-1,4,5-trisphosphate and zero extracellular calcium in brain endothelial cells J. Cell Physiol. 197 2003 205 213
    • (2003) J. Cell Physiol. , vol.197 , pp. 205-213
    • Braet, K.1    Speslagh, S.A.2    Vandamme, W.3    Willecke, K.4    Martin, P.E.5    Evans, W.H.6    Leybaert, L.7
  • 12
    • 0037285683 scopus 로고    scopus 로고
    • Photoliberating inositol-1,4,5-trisphosphate triggers ATP release that is blocked by the connexin mimetic peptide gap 26
    • K. Braet, W. Vandamme, P.E. Martin, W.H. Evans, and L. Leybaert Photoliberating inositol-1,4,5-trisphosphate triggers ATP release that is blocked by the connexin mimetic peptide gap 26 Cell Calcium 33 2003 37 48
    • (2003) Cell Calcium , vol.33 , pp. 37-48
    • Braet, K.1    Vandamme, W.2    Martin, P.E.3    Evans, W.H.4    Leybaert, L.5
  • 14
    • 40249098507 scopus 로고    scopus 로고
    • Extracellular-loop peptide antibodies reveal a predominant hemichannel organization of connexins in polarized intestinal cells
    • C. Clair, L. Combettes, F. Pierre, P. Sansonetti, and N.G. Tran Van Extracellular-loop peptide antibodies reveal a predominant hemichannel organization of connexins in polarized intestinal cells Exp. Cell Res. 314 2008 1250 1265
    • (2008) Exp. Cell Res. , vol.314 , pp. 1250-1265
    • Clair, C.1    Combettes, L.2    Pierre, F.3    Sansonetti, P.4    Tran Van N., G.5
  • 17
    • 84875503658 scopus 로고    scopus 로고
    • Negatively charged residues (Asp278 and Asp279) in the last ten amino acids of the C-terminal tail of Cx43 hemichannels are essential for loop/tail interactions
    • C. D'hondt, J. Iyyathurai, N. Wang, R. Gourdie, B. Himpens, L. Leybaert, and G. Bultynck Negatively charged residues (Asp278 and Asp279) in the last ten amino acids of the C-terminal tail of Cx43 hemichannels are essential for loop/tail interactions Biochem. Biophys. Res. Commun. 432 2013 707 712
    • (2013) Biochem. Biophys. Res. Commun. , vol.432 , pp. 707-712
    • D'Hondt, C.1    Iyyathurai, J.2    Wang, N.3    Gourdie, R.4    Himpens, B.5    Leybaert, L.6    Bultynck, G.7
  • 22
    • 33846100604 scopus 로고    scopus 로고
    • Connexin hemichannels and gap junction channels are differentially influenced by lipopolysaccharide and basic fibroblast growth factor
    • E. De Vuyst, E. Decrock, M. De Bock, H. Yamasaki, C.C. Naus, W.H. Evans, and L. Leybaert Connexin hemichannels and gap junction channels are differentially influenced by lipopolysaccharide and basic fibroblast growth factor Mol. Biol. Cell 18 2007 34 46
    • (2007) Mol. Biol. Cell , vol.18 , pp. 34-46
    • De Vuyst, E.1    Decrock, E.2    De Bock, M.3    Yamasaki, H.4    Naus, C.C.5    Evans, W.H.6    Leybaert, L.7
  • 25
  • 26
    • 84859802065 scopus 로고    scopus 로고
    • Gap26, a connexin mimetic peptide, inhibits currents carried by connexin43 hemichannels and gap junction channels
    • T. Desplantez, V. Verma, L. Leybaert, W.H. Evans, and R. Weingart Gap26, a connexin mimetic peptide, inhibits currents carried by connexin43 hemichannels and gap junction channels Pharmacol. Res. 65 2012 546 552
    • (2012) Pharmacol. Res. , vol.65 , pp. 546-552
    • Desplantez, T.1    Verma, V.2    Leybaert, L.3    Evans, W.H.4    Weingart, R.5
  • 29
    • 36649026454 scopus 로고    scopus 로고
    • Some oculodentodigital dysplasia-associated Cx43 mutations cause increased hemichannel activity in addition to deficient gap junction channels
    • R. Dobrowolski, A. Sommershof, and K. Willecke Some oculodentodigital dysplasia-associated Cx43 mutations cause increased hemichannel activity in addition to deficient gap junction channels J. Membr. Biol. 219 2007 9 17
    • (2007) J. Membr. Biol. , vol.219 , pp. 9-17
    • Dobrowolski, R.1    Sommershof, A.2    Willecke, K.3
  • 32
    • 84866729771 scopus 로고    scopus 로고
    • Manipulating connexin communication channels: Use of peptidomimetics and the translational outputs
    • W.H. Evans, G. Bultynck, and L. Leybaert Manipulating connexin communication channels: use of peptidomimetics and the translational outputs J. Membr. Biol. 245 2012 437 449
    • (2012) J. Membr. Biol. , vol.245 , pp. 437-449
    • Evans, W.H.1    Bultynck, G.2    Leybaert, L.3
  • 35
    • 34249050091 scopus 로고    scopus 로고
    • Molecular basis of voltage dependence of connexin channels: An integrative appraisal
    • D. Gonzalez, J.M. Gomez-Hernandez, and L.C. Barrio Molecular basis of voltage dependence of connexin channels: an integrative appraisal Prog. Biophys. Mol. Biol. 94 2007 66 106
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 66-106
    • Gonzalez, D.1    Gomez-Hernandez, J.M.2    Barrio, L.C.3
  • 36
  • 37
    • 0036094459 scopus 로고    scopus 로고
    • Voltage-sensing and substate rectification: Moving parts of connexin channels
    • A.L. Harris Voltage-sensing and substate rectification: moving parts of connexin channels J. Gen. Physiol. 119 2002 165 169
    • (2002) J. Gen. Physiol. , vol.119 , pp. 165-169
    • Harris, A.L.1
  • 38
    • 84865568181 scopus 로고    scopus 로고
    • Single intravenous low-dose injections of connexin 43 mimetic peptides protect ischemic heart in vivo against myocardial infarction
    • G. Hawat, P. Helie, and G. Baroudi Single intravenous low-dose injections of connexin 43 mimetic peptides protect ischemic heart in vivo against myocardial infarction J. Mol. Cell Cardiol. 53 2012 559 566
    • (2012) J. Mol. Cell Cardiol. , vol.53 , pp. 559-566
    • Hawat, G.1    Helie, P.2    Baroudi, G.3
  • 39
    • 34247157344 scopus 로고    scopus 로고
    • Characterization of the pH-dependent interaction between the gap junction protein connexin43 carboxyl terminus and cytoplasmic loop domains
    • B.J. Hirst-Jensen, P. Sahoo, F. Kieken, M. Delmar, and P.L. Sorgen Characterization of the pH-dependent interaction between the gap junction protein connexin43 carboxyl terminus and cytoplasmic loop domains J. Biol. Chem. 282 2007 5801 5813
    • (2007) J. Biol. Chem. , vol.282 , pp. 5801-5813
    • Hirst-Jensen, B.J.1    Sahoo, P.2    Kieken, F.3    Delmar, M.4    Sorgen, P.L.5
  • 40
    • 0034719104 scopus 로고    scopus 로고
    • Conversation between voltage sensors and gates of ion channels
    • R. Horn Conversation between voltage sensors and gates of ion channels Biochemistry 39 2000 15653 15658
    • (2000) Biochemistry , vol.39 , pp. 15653-15658
    • Horn, R.1
  • 41
    • 0029587218 scopus 로고
    • External barium block of Shaker potassium channels: Evidence for two binding sites
    • R.S. Hurst, R. Latorre, L. Toro, and E. Stefani External barium block of Shaker potassium channels: evidence for two binding sites J. Gen. Physiol. 106 1995 1069 1087
    • (1995) J. Gen. Physiol. , vol.106 , pp. 1069-1087
    • Hurst, R.S.1    Latorre, R.2    Toro, L.3    Stefani, E.4
  • 43
    • 77949495874 scopus 로고    scopus 로고
    • Open channel block and beyond
    • M.B. Jackson Open channel block and beyond J. Physiol. 588 2010 553 554
    • (2010) J. Physiol. , vol.588 , pp. 553-554
    • Jackson, M.B.1
  • 47
    • 84874714900 scopus 로고    scopus 로고
    • The ladder-shaped polyether toxin gambierol anchors the gating machinery of Kv3.1 channels in the resting state
    • I. Kopljar, A.J. Labro, B.T. de, J.D. Rainier, J. Tytgat, and D.J. Snyders The ladder-shaped polyether toxin gambierol anchors the gating machinery of Kv3.1 channels in the resting state J. Gen. Physiol. 141 2013 359 369
    • (2013) J. Gen. Physiol. , vol.141 , pp. 359-369
    • Kopljar, I.1    Labro, A.J.2    De, B.T.3    Rainier, J.D.4    Tytgat, J.5    Snyders, D.J.6
  • 48
    • 84866742557 scopus 로고    scopus 로고
    • The N-terminal half of the connexin protein contains the core elements of the pore and voltage gates
    • J. Kronengold, M. Srinivas, and V.K. Verselis The N-terminal half of the connexin protein contains the core elements of the pore and voltage gates J. Membr. Biol. 245 2012 453 463
    • (2012) J. Membr. Biol. , vol.245 , pp. 453-463
    • Kronengold, J.1    Srinivas, M.2    Verselis, V.K.3
  • 50
    • 0141919839 scopus 로고    scopus 로고
    • Single-channel SCAM identifies pore-lining residues in the first extracellular loop and first transmembrane domains of Cx46 hemichannels
    • J. Kronengold, E.B. Trexler, F.F. Bukauskas, T.A. Bargiello, and V.K. Verselis Single-channel SCAM identifies pore-lining residues in the first extracellular loop and first transmembrane domains of Cx46 hemichannels J. Gen. Physiol. 122 2003 389 405
    • (2003) J. Gen. Physiol. , vol.122 , pp. 389-405
    • Kronengold, J.1    Trexler, E.B.2    Bukauskas, F.F.3    Bargiello, T.A.4    Verselis, V.K.5
  • 51
    • 84858777446 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the Cx26 hemichannel: Insights into voltage-dependent loop-gating
    • T. Kwon, B. Roux, S. Jo, J.B. Klauda, A.L. Harris, and T.A. Bargiello Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating Biophys. J. 102 2012 1341 1351
    • (2012) Biophys. J. , vol.102 , pp. 1341-1351
    • Kwon, T.1    Roux, B.2    Jo, S.3    Klauda, J.B.4    Harris, A.L.5    Bargiello, T.A.6
  • 52
    • 84874742226 scopus 로고    scopus 로고
    • Voltage-dependent gating of the Cx32*43E1 hemichannel: Conformational changes at the channel entrances
    • T. Kwon, Q. Tang, and T.A. Bargiello Voltage-dependent gating of the Cx32*43E1 hemichannel: conformational changes at the channel entrances J. Gen. Physiol. 141 2013 243 259
    • (2013) J. Gen. Physiol. , vol.141 , pp. 243-259
    • Kwon, T.1    Tang, Q.2    Bargiello, T.A.3
  • 53
    • 84867135827 scopus 로고    scopus 로고
    • Being flexible: The voltage-controllable activation gate of kv channels
    • A.J. Labro, and D.J. Snyders Being flexible: the voltage-controllable activation gate of kv channels Front Pharmacol. 3 2012 168
    • (2012) Front Pharmacol. , vol.3 , pp. 168
    • Labro, A.J.1    Snyders, D.J.2
  • 54
    • 33644979261 scopus 로고    scopus 로고
    • Oculodentodigital dysplasia connexin43 mutations result in non-functional connexin hemichannels and gap junctions in C6 glioma cells
    • A. Lai, D.N. Le, W.A. Paznekas, W.D. Gifford, E.W. Jabs, and A.C. Charles Oculodentodigital dysplasia connexin43 mutations result in non-functional connexin hemichannels and gap junctions in C6 glioma cells J. Cell Sci. 119 2006 532 541
    • (2006) J. Cell Sci. , vol.119 , pp. 532-541
    • Lai, A.1    Le, D.N.2    Paznekas, W.A.3    Gifford, W.D.4    Jabs, E.W.5    Charles, A.C.6
  • 56
    • 33747348967 scopus 로고    scopus 로고
    • Nanomechanics of hemichannel conformations: Connexin flexibility underlying channel opening and closing
    • F. Liu, F.T. Arce, S. Ramachandran, and R. Lal Nanomechanics of hemichannel conformations: connexin flexibility underlying channel opening and closing J. Biol. Chem. 281 2006 23207 23217
    • (2006) J. Biol. Chem. , vol.281 , pp. 23207-23217
    • Liu, F.1    Arce, F.T.2    Ramachandran, S.3    Lal, R.4
  • 57
    • 69849103802 scopus 로고    scopus 로고
    • Connexin channels and phospholipids: Association and modulation
    • D. Locke, and A.L. Harris Connexin channels and phospholipids: association and modulation BMC. Biol. 7 2009 52
    • (2009) BMC. Biol. , vol.7 , pp. 52
    • Locke, D.1    Harris, A.L.2
  • 58
    • 80054013332 scopus 로고    scopus 로고
    • Mechanism for modulation of gating of connexin26-containing channels by taurine
    • D. Locke, F. Kieken, L. Tao, P.L. Sorgen, and A.L. Harris Mechanism for modulation of gating of connexin26-containing channels by taurine J. Gen. Physiol. 138 2011 321 339
    • (2011) J. Gen. Physiol. , vol.138 , pp. 321-339
    • Locke, D.1    Kieken, F.2    Tao, L.3    Sorgen, P.L.4    Harris, A.L.5
  • 59
    • 25444475775 scopus 로고    scopus 로고
    • Lipid rafts prepared by different methods contain different connexin channels, but gap junctions are not lipid rafts
    • D. Locke, J. Liu, and A.L. Harris Lipid rafts prepared by different methods contain different connexin channels, but gap junctions are not lipid rafts Biochemistry 44 2005 13027 13042
    • (2005) Biochemistry , vol.44 , pp. 13027-13042
    • Locke, D.1    Liu, J.2    Harris, A.L.3
  • 60
    • 84880000898 scopus 로고    scopus 로고
    • Insights on the mechanisms of Ca2+ regulation of connexin26 hemichannels revealed by human pathogenic mutations (D50N/Y)
    • W. Lopez, J. Gonzalez, Y. Liu, A.L. Harris, and J.E. Contreras Insights on the mechanisms of Ca2+ regulation of connexin26 hemichannels revealed by human pathogenic mutations (D50N/Y) J. Gen. Physiol. 142 2013 23 35
    • (2013) J. Gen. Physiol. , vol.142 , pp. 23-35
    • Lopez, W.1    Gonzalez, J.2    Liu, Y.3    Harris, A.L.4    Contreras, J.E.5
  • 61
    • 0242426633 scopus 로고    scopus 로고
    • Calmodulin and protein kinase C regulate gap junctional coupling in lens epithelial cells
    • M.M. Lurtz, and C.F. Louis Calmodulin and protein kinase C regulate gap junctional coupling in lens epithelial cells Am. J. Physiol. Cell Physiol. 285 2003 C1475 C1482
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Lurtz, M.M.1    Louis, C.F.2
  • 63
    • 80052056976 scopus 로고    scopus 로고
    • Structure analysis of human gap junction channel
    • S. Maeda Structure analysis of human gap junction channel Seikagaku 83 2011 36 40
    • (2011) Seikagaku , vol.83 , pp. 36-40
    • Maeda, S.1
  • 65
    • 0037099393 scopus 로고    scopus 로고
    • Conformational changes in surface structures of isolated connexin 26 gap junctions
    • D.J. Muller, G.M. Hand, A. Engel, and G.E. Sosinsky Conformational changes in surface structures of isolated connexin 26 gap junctions EMBO J. 21 2002 3598 3607
    • (2002) EMBO J. , vol.21 , pp. 3598-3607
    • Muller, D.J.1    Hand, G.M.2    Engel, A.3    Sosinsky, G.E.4
  • 66
    • 48449084169 scopus 로고    scopus 로고
    • Connexin 43 mimetic peptides reduce swelling, astrogliosis, and neuronal cell death after spinal cord injury
    • S.J. O'Carroll, M. Alkadhi, L.F. Nicholson, and C.R. Green Connexin 43 mimetic peptides reduce swelling, astrogliosis, and neuronal cell death after spinal cord injury Cell Commun. Adhes. 15 2008 27 42
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 27-42
    • O'Carroll, S.J.1    Alkadhi, M.2    Nicholson, L.F.3    Green, C.R.4
  • 67
    • 84875956067 scopus 로고    scopus 로고
    • Connexin43 mimetic peptide is neuroprotective and improves function following spinal cord injury
    • Epub ahead of print
    • S.J. O'Carroll, C.A. Gorrie, S. Velamoor, C.R. Green, and L.F. Nicholson Connexin43 mimetic peptide is neuroprotective and improves function following spinal cord injury Neurosci. Res. 2013 Epub ahead of print
    • (2013) Neurosci. Res.
    • O'Carroll, S.J.1    Gorrie, C.A.2    Velamoor, S.3    Green, C.R.4    Nicholson, L.F.5
  • 68
  • 69
    • 0036393541 scopus 로고    scopus 로고
    • Gap junction intercellular communication during lymphocyte transendothelial migration
    • E. Oviedo-Orta, R.J. Errington, and W.H. Evans Gap junction intercellular communication during lymphocyte transendothelial migration Cell Biol. Int. 26 2002 253 263
    • (2002) Cell Biol. Int. , vol.26 , pp. 253-263
    • Oviedo-Orta, E.1    Errington, R.J.2    Evans, W.H.3
  • 70
    • 19544379905 scopus 로고    scopus 로고
    • ATP released via gap junction hemichannels from the pigment epithelium regulates neural retinal progenitor proliferation
    • R.A. Pearson, N. Dale, E. Llaudet, and P. Mobbs ATP released via gap junction hemichannels from the pigment epithelium regulates neural retinal progenitor proliferation Neuron 46 2005 731 744
    • (2005) Neuron , vol.46 , pp. 731-744
    • Pearson, R.A.1    Dale, N.2    Llaudet, E.3    Mobbs, P.4
  • 71
    • 1642385314 scopus 로고    scopus 로고
    • Chemical gating of gap junction channels; Roles of calcium, pH and calmodulin
    • C. Peracchia Chemical gating of gap junction channels; roles of calcium, pH and calmodulin Biochim. Biophys. Acta 1662 2004 61 80
    • (2004) Biochim. Biophys. Acta , vol.1662 , pp. 61-80
    • Peracchia, C.1
  • 72
    • 0032913131 scopus 로고    scopus 로고
    • Gating of cx46 gap junction hemichannels by calcium and voltage
    • A. Pfahnl, and G. Dahl Gating of cx46 gap junction hemichannels by calcium and voltage Pflugers Arch. 437 1999 345 353
    • (1999) Pflugers Arch. , vol.437 , pp. 345-353
    • Pfahnl, A.1    Dahl, G.2
  • 74
    • 84863533459 scopus 로고    scopus 로고
    • The contractile system as a negative regulator of the connexin 43 hemichannel
    • R. Ponsaerts, N. Wang, B. Himpens, L. Leybaert, and G. Bultynck The contractile system as a negative regulator of the connexin 43 hemichannel Biol. Cell 104 2012 367 377
    • (2012) Biol. Cell , vol.104 , pp. 367-377
    • Ponsaerts, R.1    Wang, N.2    Himpens, B.3    Leybaert, L.4    Bultynck, G.5
  • 75
    • 0034611012 scopus 로고    scopus 로고
    • Physiological role of gap-junctional hemichannels. Extracellular calcium-dependent isosmotic volume regulation
    • A.P. Quist, S.K. Rhee, H. Lin, and R. Lal Physiological role of gap-junctional hemichannels. Extracellular calcium-dependent isosmotic volume regulation J. Cell Biol. 148 2000 1063 1074
    • (2000) J. Cell Biol. , vol.148 , pp. 1063-1074
    • Quist, A.P.1    Rhee, S.K.2    Lin, H.3    Lal, R.4
  • 76
    • 37249015389 scopus 로고    scopus 로고
    • Cx43 hemichannels and gap junction channels in astrocytes are regulated oppositely by proinflammatory cytokines released from activated microglia
    • M.A. Retamal, N. Froger, N. Palacios-Prado, P. Ezan, P.J. Saez, J.C. Saez, and C. Giaume Cx43 hemichannels and gap junction channels in astrocytes are regulated oppositely by proinflammatory cytokines released from activated microglia J. Neurosci. 27 2007 13781 13792
    • (2007) J. Neurosci. , vol.27 , pp. 13781-13792
    • Retamal, M.A.1    Froger, N.2    Palacios-Prado, N.3    Ezan, P.4    Saez, P.J.5    Saez, J.C.6    Giaume, C.7
  • 80
    • 77954320871 scopus 로고    scopus 로고
    • 2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome
    • 2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome J. Gen. Physiol. 136 2010 47 62
    • (2010) J. Gen. Physiol. , vol.136 , pp. 47-62
    • Sanchez, H.A.1    Mese, G.2    Srinivas, M.3    White, T.W.4    Verselis, V.K.5
  • 81
    • 84880004378 scopus 로고    scopus 로고
    • The D50N mutation and syndromic deafness: Altered Cx26 hemichannel properties caused by effects on the pore and intersubunit interactions
    • H.A. Sanchez, K. Villone, M. Srinivas, and V.K. Verselis The D50N mutation and syndromic deafness: altered Cx26 hemichannel properties caused by effects on the pore and intersubunit interactions J. Gen. Physiol. 142 2013 3 22
    • (2013) J. Gen. Physiol. , vol.142 , pp. 3-22
    • Sanchez, H.A.1    Villone, K.2    Srinivas, M.3    Verselis, V.K.4
  • 82
    • 0032608043 scopus 로고    scopus 로고
    • Commentary: A revised view of local anesthetic action: What channel state is really stabilized?
    • T. Scheuer Commentary: a revised view of local anesthetic action: what channel state is really stabilized? J. Gen. Physiol. 113 1999 3 6
    • (1999) J. Gen. Physiol. , vol.113 , pp. 3-6
    • Scheuer, T.1
  • 83
    • 0036064899 scopus 로고    scopus 로고
    • Mechanisms of (local) anaesthetics on voltage-gated sodium and other ion channels
    • A. Scholz Mechanisms of (local) anaesthetics on voltage-gated sodium and other ion channels Br. J. Anaesth. 89 2002 52 61
    • (2002) Br. J. Anaesth. , vol.89 , pp. 52-61
    • Scholz, A.1
  • 84
    • 15744376289 scopus 로고    scopus 로고
    • Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region
    • A. Seki, H.S. Duffy, W. Coombs, D.C. Spray, S.M. Taffet, and M. Delmar Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region Circ. Res. 95 2004 e22 e28
    • (2004) Circ. Res. , vol.95
    • Seki, A.1    Duffy, H.S.2    Coombs, W.3    Spray, D.C.4    Taffet, S.M.5    Delmar, M.6
  • 86
    • 20444397467 scopus 로고    scopus 로고
    • Correlative studies of gating in Cx46 and Cx50 hemichannels and gap junction channels
    • M. Srinivas, J. Kronengold, F.F. Bukauskas, T.A. Bargiello, and V.K. Verselis Correlative studies of gating in Cx46 and Cx50 hemichannels and gap junction channels Biophys. J. 88 2005 1725 1739
    • (2005) Biophys. J. , vol.88 , pp. 1725-1739
    • Srinivas, M.1    Kronengold, J.2    Bukauskas, F.F.3    Bargiello, T.A.4    Verselis, V.K.5
  • 87
    • 33846444703 scopus 로고    scopus 로고
    • Tarantula toxins interacting with voltage sensors in potassium channels
    • K.J. Swartz Tarantula toxins interacting with voltage sensors in potassium channels Toxicon 49 2007 213 230
    • (2007) Toxicon , vol.49 , pp. 213-230
    • Swartz, K.J.1
  • 88
    • 66749118906 scopus 로고    scopus 로고
    • Conformational changes in a pore-forming region underlie voltage-dependent "loop gating" of an unapposed connexin hemichannel
    • Q. Tang, T.L. Dowd, V.K. Verselis, and T.A. Bargiello Conformational changes in a pore-forming region underlie voltage-dependent "loop gating" of an unapposed connexin hemichannel J. Gen. Physiol. 133 2009 555 570
    • (2009) J. Gen. Physiol. , vol.133 , pp. 555-570
    • Tang, Q.1    Dowd, T.L.2    Verselis, V.K.3    Bargiello, T.A.4
  • 91
    • 77957256186 scopus 로고    scopus 로고
    • Design and characterization of the first peptidomimetic molecule that prevents acidification-induced closure of cardiac gap junctions
    • V. Verma, B.D. Larsen, W. Coombs, X. Lin, E. Sarrou, S.M. Taffet, and M. Delmar Design and characterization of the first peptidomimetic molecule that prevents acidification-induced closure of cardiac gap junctions Heart Rhythm. 7 2010 1491 1498
    • (2010) Heart Rhythm. , vol.7 , pp. 1491-1498
    • Verma, V.1    Larsen, B.D.2    Coombs, W.3    Lin, X.4    Sarrou, E.5    Taffet, S.M.6    Delmar, M.7
  • 93
    • 50449110491 scopus 로고    scopus 로고
    • Divalent cations regulate connexin hemichannels by modulating intrinsic voltage-dependent gating
    • V.K. Verselis, and M. Srinivas Divalent cations regulate connexin hemichannels by modulating intrinsic voltage-dependent gating J. Gen. Physiol. 132 2008 315 327
    • (2008) J. Gen. Physiol. , vol.132 , pp. 315-327
    • Verselis, V.K.1    Srinivas, M.2
  • 94
    • 84890441799 scopus 로고    scopus 로고
    • Connexin channel modulators and their mechanisms of action
    • Epub ahead of print
    • V.K. Verselis, and M. Srinivas Connexin channel modulators and their mechanisms of action Neuropharmacology 2013 Epub ahead of print
    • (2013) Neuropharmacology
    • Verselis, V.K.1    Srinivas, M.2
  • 95
    • 63249084923 scopus 로고    scopus 로고
    • Loop gating of connexin hemichannels involves movement of pore-lining residues in the first extracellular loop domain
    • V.K. Verselis, M.P. Trelles, C. Rubinos, T.A. Bargiello, and M. Srinivas Loop gating of connexin hemichannels involves movement of pore-lining residues in the first extracellular loop domain J. Biol. Chem. 284 2009 4484 4493
    • (2009) J. Biol. Chem. , vol.284 , pp. 4484-4493
    • Verselis, V.K.1    Trelles, M.P.2    Rubinos, C.3    Bargiello, T.A.4    Srinivas, M.5
  • 96
    • 34548764500 scopus 로고    scopus 로고
    • Modulation of membrane channel currents by gap junction protein mimetic peptides: Size matters
    • J. Wang, M. Ma, S. Locovei, R.W. Keane, and G. Dahl Modulation of membrane channel currents by gap junction protein mimetic peptides: size matters Am. J. Physiol. Cell Physiol. 293 2007 C1112 C1119
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Wang, J.1    Ma, M.2    Locovei, S.3    Keane, R.W.4    Dahl, G.5
  • 100
    • 62449100273 scopus 로고    scopus 로고
    • Connexin mimetic peptides improve cell migration rates of human epidermal keratinocytes and dermal fibroblasts in vitro
    • C.S. Wright, M.A. van Steensel, M.B. Hodgins, and P.E. Martin Connexin mimetic peptides improve cell migration rates of human epidermal keratinocytes and dermal fibroblasts in vitro Wound Repair Regen 17 2009 240 249
    • (2009) Wound Repair Regen , vol.17 , pp. 240-249
    • Wright, C.S.1    Van Steensel, M.A.2    Hodgins, M.B.3    Martin, P.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.